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Literature summary extracted from

  • Chavez-Bejar, M.I.; Lara, A.R.; Lopez, H.; Hernandez-Chavez, G.; Martinez, A.; Ramirez, O.T.; Bolivar, F.; Gosset, G.
    Metabolic engineering of Escherichia coli for L-tyrosine production by expression of genes coding for the chorismate mutase domain of the native chorismate mutase-prephenate dehydratase and a cyclohexadienyl dehydrogenase from Zymomonas mobilis (2008), Appl. Environ. Microbiol., 74, 3284-3290.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.12 expressed in Escherichia coli Zymomonas mobilis
4.2.1.51 expressed in Escherichia coli, PB12 strain, pCR-BluntII-TOPO, additional strains and plasmids listed Zymomonas mobilis
5.4.99.5 expressed in Escherichia coli strain FA114 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.12 L-Tyr L-Tyr inhibits TyrAp activity by 90% at concentrations higher than 0.5 mM Zymomonas mobilis
1.3.1.79 additional information TyrC is not sensitive to L-Tyr inhibition Zymomonas mobilis

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.12 Zymomonas mobilis
-
-
-
1.3.1.79 Zymomonas mobilis
-
strain ATCC 31821
-
4.2.1.51 Zymomonas mobilis Q5NLV8 encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
-
4.2.1.51 Zymomonas mobilis ATCC 31821 Q5NLV8 encoded by pheA (ZMO1678) gene; ATCC 31821 wild-type strain
-
5.4.99.5 Escherichia coli
-
-
-
5.4.99.5 Escherichia coli JM101
-
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.79 additional information
-
TyrC has a specific activity of 1.54 IU/mg protein, while in the presence of 0.6 mM L-Tyr the specific activity was 1.34 IU/mg protein Zymomonas mobilis
4.2.1.51 additional information
-
comparison of prephenate dehydratase isolated from Zymomonas mobilis to those of Escherichia coli with regard to the capacity to produce L-tyrosine in Escherichia coli strains modified to increase the carbon flow to chorismate, kinetic and stoichiometric parameters determined in shake flask experiments, parameters determined from data generated in bioreactor experiments, possibility to employ feedback inhibition-insensitive enzymes for strain development as part of a metabolic engineering strategy for L-tyrosine production Zymomonas mobilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.12 prephenate + NAD+
-
Zymomonas mobilis 4-hydroxyphenylpyruvate + NADH + CO2
-
?
1.3.1.79 L-arogenate + NAD(P)+
-
Zymomonas mobilis L-tyrosine + NAD(P)H + CO2
-
?
1.3.1.79 prephenate + NAD(P)+
-
Zymomonas mobilis p-hydroxyphenylpyruvate + NAD(P)H + CO2
-
?
5.4.99.5 Chorismate
-
Escherichia coli Prephenate
-
?
5.4.99.5 Chorismate
-
Escherichia coli JM101 Prephenate
-
?

Synonyms

EC Number Synonyms Comment Organism
1.3.1.12 chorismate mutase-prephenate dehydratase
-
Zymomonas mobilis
1.3.1.12 CM-TyrAp
-
Zymomonas mobilis
1.3.1.79 cyclohexadienyl dehydrogenase
-
Zymomonas mobilis
1.3.1.79 TyrAc
-
Zymomonas mobilis
1.3.1.79 TyrC
-
Zymomonas mobilis
5.4.99.5 chorismate mutase-prephenate dehydrogenase bifunctional enzyme Escherichia coli
5.4.99.5 CM-prephenate dehydratase bifunctional enzyme Escherichia coli
5.4.99.5 CM-TyrAp bifunctional enzyme Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.12 NAD+
-
Zymomonas mobilis
1.3.1.79 NAD(P)+
-
Zymomonas mobilis